Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A3KCL7 (OXDD_PIG)

Last modified October 13, 2009. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    D-aspartate oxidase
      Short name=DASOX
    EC=1.4.3.1
Alternative name(s):
    DDO
Gene names
Name: DDO
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Hide | Top

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

Hide | Top

General annotation (Comments)

Function

Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate By similarity.

Catalytic activity

D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2.

Cofactor

FAD or 6-hydroxyflavin adenine dinucleotide By similarity.

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the DAMOX/DASOX family.

Hide | Top

Ontologies

Keywords
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionD-amino-acid oxidase activity

Inferred from electronic annotation. Source: InterPro

D-aspartate oxidase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341D-aspartate oxidase
PRO_0000330729

Regions

Nucleotide binding6 – 2015FAD By similarity
Nucleotide binding36 – 372FAD By similarity
Nucleotide binding43 – 442FAD By similarity
Nucleotide binding48 – 503FAD By similarity
Nucleotide binding307 – 3115FAD By similarity
Motif339 – 3413Microbody targeting signal Potential

Sites

Binding site1661FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1831FAD By similarity
Binding site2231Substrate By similarity
Binding site2781Substrate By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
A3KCL7-1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 97AFE48AD15A0D23

FASTA34137,316
        10         20         30         40         50         60 
MDTVRIAVVG AGVMGLSTAV CIFKLVPGCS ITVISDKFTP ETTSDVAAGM LIPPVYPDTP 

        70         80         90        100        110        120 
IHKQKQWFKD TFDHLFAIAN SAEAKDAGVL LVSGWQIFQS APTEEVPFWA DVVLGFRKMT 

       130        140        150        160        170        180 
KNELKKFPQH VCGQAFTTLK YEGPTYLPWL EKRVKGSGGL VLTRRVEDLW ELHPSFDIVV 

       190        200        210        220        230        240 
NCSGLGSKQL VGDMDIFPVR GQVLKVQAPW VKHFIRDGSG LTYIYPGLAN VTLGGTRQKG 

       250        260        270        280        290        300 
DWNLSPNAEI SKQILSRCCA LEPSLRGACD IREKVGLRPS RPGVRLEKEL LVQGSQRLPV 

       310        320        330        340 
VHNYGHGSGG IAMHWGTALE AARLVSECVQ ALRTPAPKSK L

« Hide

Hide | Top

References

[1]"Purification, cDNA cloning and characterization of D-aspartate oxidase from porcine kidney."
Yamamoto A., Tanaka H., Ishida T., Horiike K.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.

Hide | Top

Cross-references

Sequence databases

AB271762 mRNA. Translation: BAF47961.1.
RefSeqNP_001090895.1.
UniGeneSsc.40562

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID100037287.
KEGGssc:100037287.

Organism-specific databases

CTD100037287.

Family and domain databases

InterProIPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01266. DAO. 1 hit.
[Graphical view]
PROSITEPS00677. DAO. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameOXDD_PIG
AccessionPrimary (citable) accession number: A3KCL7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 3, 2007
Last modified: October 13, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents